skip to main content
Language:
Search Limited to: Search Limited to: Resource type Show Results with: Show Results with: Search type Index

Results 1 - 20 of 127  for All Library Resources

Results 1 2 3 4 5 next page
Show only
Result Number Material Type Add to My Shelf Action Record Details and Options
1
Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein
Material Type:
Article
Add to My Research

Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein

Cell, 2020-04, Vol.181 (2), p.281-292.e6 [Peer Reviewed Journal]

2020 Elsevier Inc. ;Copyright © 2020 Elsevier Inc. All rights reserved. ;2020. Not withstanding the ProQuest Terms and Conditions, you may use this content in accordance with the associated terms available at https://www.elsevier.com/legal/elsevier-website-terms-and-conditions ;Distributed under a Creative Commons Attribution 4.0 International License ;2020 Elsevier Inc. 2020 Elsevier Inc. ;ISSN: 0092-8674 ;EISSN: 1097-4172 ;DOI: 10.1016/j.cell.2020.02.058 ;PMID: 32155444

Digital Resources/Online E-Resources

2
Structure-guided covalent stabilization of coronavirus spike glycoprotein trimers in the closed conformation
Material Type:
Article
Add to My Research

Structure-guided covalent stabilization of coronavirus spike glycoprotein trimers in the closed conformation

Nature structural & molecular biology, 2020-10, Vol.27 (10), p.942-949 [Peer Reviewed Journal]

COPYRIGHT 2020 Nature Publishing Group ;The Author(s) 2020 ;ISSN: 1545-9993 ;EISSN: 1545-9985 ;DOI: 10.1038/s41594-020-0483-8 ;PMID: 32753755

Full text available

3
Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion
Material Type:
Article
Add to My Research

Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion

Proceedings of the National Academy of Sciences - PNAS, 2017-10, Vol.114 (42), p.11157-11162 [Peer Reviewed Journal]

Volumes 1–89 and 106–114, copyright as a collective work only; author(s) retains copyright to individual articles ;Copyright National Academy of Sciences Oct 17, 2017 ;Distributed under a Creative Commons Attribution 4.0 International License ;ISSN: 0027-8424 ;EISSN: 1091-6490 ;DOI: 10.1073/pnas.1708727114 ;PMID: 29073020

Full text available

4
De novo design of picomolar SARS-CoV-2 miniprotein inhibitors
Material Type:
Article
Add to My Research

De novo design of picomolar SARS-CoV-2 miniprotein inhibitors

Science, 2020-10, Vol.370 (6515) [Peer Reviewed Journal]

2020. This work is published under https://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;DOI: 10.1126/science.abd9909

Digital Resources/Online E-Resources

5
Deep Mutational Scanning of SARS-CoV-2 Receptor Binding Domain Reveals Constraints on Folding and ACE2 Binding
Material Type:
Article
Add to My Research

Deep Mutational Scanning of SARS-CoV-2 Receptor Binding Domain Reveals Constraints on Folding and ACE2 Binding

Cell, 2020-09, Vol.182 (5), p.1295-1310.e20 [Peer Reviewed Journal]

2020 The Author(s) ;Copyright © 2020 The Author(s). Published by Elsevier Inc. All rights reserved. ;2020. Not withstanding the ProQuest Terms and Conditions, you may use this content in accordance with the associated terms available at https://www.elsevier.com/legal/elsevier-website-terms-and-conditions ;Distributed under a Creative Commons Attribution 4.0 International License ;2020 The Author(s) 2020 ;ISSN: 0092-8674 ;EISSN: 1097-4172 ;DOI: 10.1016/j.cell.2020.08.012 ;PMID: 32841599

Digital Resources/Online E-Resources

6
Structural basis for human coronavirus attachment to sialic acid receptors
Material Type:
Article
Add to My Research

Structural basis for human coronavirus attachment to sialic acid receptors

Nature Structural & Molecular Biology, 2019-06, Vol.26 (6), p.481-489 [Peer Reviewed Journal]

COPYRIGHT 2019 Nature Publishing Group ;The Author(s), under exclusive licence to Springer Nature America, Inc. 2019. ;2019. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the associated terms available at https://www.springernature.com/gp/researchers/campaigns/coronavirus ;Distributed under a Creative Commons Attribution 4.0 International License ;The Author(s), under exclusive licence to Springer Nature America, Inc. 2019 ;ISSN: 1545-9993 ;EISSN: 1545-9985 ;DOI: 10.1038/s41594-019-0233-y ;PMID: 31160783

Digital Resources/Online E-Resources

7
Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion
Material Type:
Article
Add to My Research

Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion

Cell, 2019-02, Vol.176 (5), p.1026-1039.e15 [Peer Reviewed Journal]

2018 Elsevier Inc. ;Copyright © 2018 Elsevier Inc. All rights reserved. ;2019. Not withstanding the ProQuest Terms and Conditions, you may use this content in accordance with the associated terms available at https://www.elsevier.com/legal/elsevier-website-terms-and-conditions ;Distributed under a Creative Commons Attribution 4.0 International License ;2018 Elsevier Inc. 2018 Elsevier Inc. ;ISSN: 0092-8674 ;EISSN: 1097-4172 ;DOI: 10.1016/j.cell.2018.12.028 ;PMID: 30712865

Digital Resources/Online E-Resources

8
Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy
Material Type:
Article
Add to My Research

Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy

Nature structural & molecular biology, 2016-10, Vol.23 (10), p.899-905 [Peer Reviewed Journal]

COPYRIGHT 2016 Nature Publishing Group ;COPYRIGHT 2016 Nature Publishing Group ;Distributed under a Creative Commons Attribution 4.0 International License ;Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved. 2016 ;ISSN: 1545-9993 ;EISSN: 1545-9985 ;DOI: 10.1038/nsmb.3293 ;PMID: 27617430

Full text available

9
SARS-CoV-2 immune evasion by the B.1.427/B.1.429 variant of concern
Material Type:
Article
Add to My Research

SARS-CoV-2 immune evasion by the B.1.427/B.1.429 variant of concern

Science, 2021-08, Vol.373 (6555) [Peer Reviewed Journal]

2021. This work is published under https://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;DOI: 10.1126/science.abi7994

Digital Resources/Online E-Resources

10
SARS-CoV-2 breakthrough infections elicit potent, broad, and durable neutralizing antibody responses
Material Type:
Article
Add to My Research

SARS-CoV-2 breakthrough infections elicit potent, broad, and durable neutralizing antibody responses

Cell, 2022-03, Vol.185 (5), p.872-880.e3 [Peer Reviewed Journal]

2022 Elsevier Inc. ;Copyright © 2022 Elsevier Inc. All rights reserved. ;2022 Elsevier Inc. 2022 Elsevier Inc. ;ISSN: 0092-8674 ;EISSN: 1097-4172 ;DOI: 10.1016/j.cell.2022.01.011 ;PMID: 35123650

Full text available

11
Lectins enhance SARS-CoV-2 infection and influence neutralizing antibodies
Material Type:
Article
Add to My Research

Lectins enhance SARS-CoV-2 infection and influence neutralizing antibodies

Nature (London), 2021-10, Vol.598 (7880), p.342-347 [Peer Reviewed Journal]

2021. The Author(s), under exclusive licence to Springer Nature Limited. ;COPYRIGHT 2021 Nature Publishing Group ;Copyright Nature Publishing Group Oct 14, 2021 ;ISSN: 0028-0836 ;EISSN: 1476-4687 ;DOI: 10.1038/s41586-021-03925-1 ;PMID: 34464958

Full text available

12
Deep mutational scans for ACE2 binding, RBD expression, and antibody escape in the SARS-CoV-2 Omicron BA.1 and BA.2 receptor-binding domains
Material Type:
Article
Add to My Research

Deep mutational scans for ACE2 binding, RBD expression, and antibody escape in the SARS-CoV-2 Omicron BA.1 and BA.2 receptor-binding domains

PLoS pathogens, 2022-11, Vol.18 (11), p.e1010951-e1010951 [Peer Reviewed Journal]

Copyright: © 2022 Starr et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. ;COPYRIGHT 2022 Public Library of Science ;2022 Starr et al 2022 Starr et al ;ISSN: 1553-7374 ;ISSN: 1553-7366 ;EISSN: 1553-7374 ;DOI: 10.1371/journal.ppat.1010951 ;PMID: 36399443

Full text available

13
Structural basis for broad coronavirus neutralization
Material Type:
Article
Add to My Research

Structural basis for broad coronavirus neutralization

Nature structural & molecular biology, 2021-06, Vol.28 (6), p.478-486 [Peer Reviewed Journal]

The Author(s), under exclusive licence to Springer Nature America, Inc. 2021. ;ISSN: 1545-9993 ;EISSN: 1545-9985 ;DOI: 10.1038/s41594-021-00596-4 ;PMID: 33981021

Full text available

14
Discovery and characterization of spike N-terminal domain-binding aptamers for rapid SARS-CoV-2 detection
Material Type:
Article
Add to My Research

Discovery and characterization of spike N-terminal domain-binding aptamers for rapid SARS-CoV-2 detection

Angewandte Chemie International Edition, 2021-09 [Peer Reviewed Journal]

2021. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the associated terms available at https://novel-coronavirus.onlinelibrary.wiley.com ;DOI: 10.1002/anie.202107730

Digital Resources/Online E-Resources

15
Serological identification of SARS-CoV-2 infections among children visiting a hospital during the initial Seattle outbreak
Material Type:
Article
Add to My Research

Serological identification of SARS-CoV-2 infections among children visiting a hospital during the initial Seattle outbreak

Nature communications, 2020-09, Vol.11 (1), p.4378-4378, Article 4378 [Peer Reviewed Journal]

The Author(s) 2020. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;The Author(s) 2020 ;ISSN: 2041-1723 ;EISSN: 2041-1723 ;DOI: 10.1038/s41467-020-18178-1 ;PMID: 32873791

Full text available

16
Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein
Material Type:
Article
Add to My Research

Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein

Cell, 2020-12, Vol.183 (6), p.1735-1735 [Peer Reviewed Journal]

2020 Elsevier Inc. ;2020 Elsevier Inc. 2020 Elsevier Inc. ;ISSN: 0092-8674 ;EISSN: 1097-4172 ;DOI: 10.1016/j.cell.2020.11.032 ;PMID: 33306958

Full text available

17
Subunit connectivity, assembly determinants and architecture of the yeast exocyst complex
Material Type:
Article
Add to My Research

Subunit connectivity, assembly determinants and architecture of the yeast exocyst complex

Nature structural & molecular biology, 2016-01, Vol.23 (1), p.59-66 [Peer Reviewed Journal]

COPYRIGHT 2016 Nature Publishing Group ;COPYRIGHT 2016 Nature Publishing Group ;ISSN: 1545-9993 ;EISSN: 1545-9985 ;DOI: 10.1038/nsmb.3146 ;PMID: 26656853

Full text available

18
Secreted Effectors Encoded within and outside of the Francisella Pathogenicity Island Promote Intramacrophage Growth
Material Type:
Article
Add to My Research

Secreted Effectors Encoded within and outside of the Francisella Pathogenicity Island Promote Intramacrophage Growth

Cell host & microbe, 2016-11, Vol.20 (5), p.573-583 [Peer Reviewed Journal]

2016 Elsevier Inc. ;Copyright © 2016 Elsevier Inc. All rights reserved. ;ISSN: 1931-3128 ;EISSN: 1934-6069 ;DOI: 10.1016/j.chom.2016.10.008 ;PMID: 27832588

Full text available

19
Safety and immunogenicity of a SARS-CoV-2 recombinant protein nanoparticle vaccine (GBP510) adjuvanted with AS03: A randomised, placebo-controlled, observer-blinded phase 1/2 trial
Material Type:
Article
Add to My Research

Safety and immunogenicity of a SARS-CoV-2 recombinant protein nanoparticle vaccine (GBP510) adjuvanted with AS03: A randomised, placebo-controlled, observer-blinded phase 1/2 trial

EClinicalMedicine, 2022-09, Vol.51, p.101569-101569, Article 101569 [Peer Reviewed Journal]

2022 The Authors ;2022 Published by Elsevier Ltd. 2022 ;ISSN: 2589-5370 ;EISSN: 2589-5370 ;DOI: 10.1016/j.eclinm.2022.101569 ;PMID: 35879941

Full text available

20
Structural changes in the SARS-CoV-2 spike E406W mutant escaping a clinical monoclonal antibody cocktail
Material Type:
Article
Add to My Research

Structural changes in the SARS-CoV-2 spike E406W mutant escaping a clinical monoclonal antibody cocktail

Cell reports (Cambridge), 2023-06, Vol.42 (6), p.112621-112621, Article 112621 [Peer Reviewed Journal]

2023 The Authors ;Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved. ;ISSN: 2211-1247 ;EISSN: 2211-1247 ;DOI: 10.1016/j.celrep.2023.112621 ;PMID: 37300832

Full text available

Results 1 - 20 of 127  for All Library Resources

Results 1 2 3 4 5 next page

Personalize your results

  1. Edit

Refine Search Results

Expand My Results

  1.   

Show only

  1. Peer-reviewed Journals (69)

Refine My Results

New Records 

  1. New From Last Month  (13)
  2. More options open sub menu

Resource Type 

  1. Articles  (101)
  2. Patents  (22)
  3. Text Resources  (3)
  4. Web Resources  (1)
  5. More options open sub menu

Language 

  1. English  (118)
  2. Japanese  (25)
  3. French  (7)
  4. Spanish  (5)
  5. German  (4)
  6. Korean  (3)
  7. Portuguese  (2)
  8. More options open sub menu

Searching Remote Databases, Please Wait